Structural highlights
Function
ELBP_ECOLX The biological activity of the toxin is produced by the A chain, which activates intracellular adenyl cyclase.
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The galactose-binding site in cholera toxin and the closely related heat-labile enterotoxin (LT) from Escherichia coli is an attractive target for the rational design of potential anti-cholera drugs. In this paper we analyse the molecular structure of this binding site as seen in several crystal structures, including that of an LT:galactose complex which we report here at 2.2 A resolution. The binding surface on the free toxin contains several tightly associated water molecules and a relatively flexible loop consisting of residues 51-60 of the B subunit. During receptor binding this loop becomes tightly ordered by forming hydrogen bonds jointly to the GM1 pentasaccharide and to a set of water molecules which stabilize the toxin:receptor complex.
Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT).,Merritt EA, Sixma TK, Kalk KH, van Zanten BA, Hol WG Mol Microbiol. 1994 Aug;13(4):745-53. PMID:7997185[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Merritt EA, Sixma TK, Kalk KH, van Zanten BA, Hol WG. Galactose-binding site in Escherichia coli heat-labile enterotoxin (LT) and cholera toxin (CT). Mol Microbiol. 1994 Aug;13(4):745-53. PMID:7997185
